CD61

From Wikipedia, the free encyclopedia

Integrin, beta 3 (platelet glycoprotein IIIa, antigen CD61)

PDB rendering based on 1jv2.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1JV2, 1KUP, 1KUZ, 1L5G, 1M1X, 1M8O, 1MIZ, 1MK7, 1MK9, 1S4X, 1TYE, 1U8C, 2K9J, 2KNC, 2KV9, 2L1C, 2L91, 2LJD, 2LJE, 2LJF, 2Q6W, 2RMZ, 2RN0, 2VC2, 2VDK, 2VDL, 2VDM, 2VDN, 2VDO, 2VDP, 2VDQ, 2VDR, 3FCS, 3FCU, 3IJE, 3NID, 3NIF, 3NIG, 3T3M, 3T3P, 3ZDX, 3ZDY, 3ZDZ, 3ZE0, 3ZE1, 3ZE2, 4CAK, 4G1E, 4G1M

Identifiers

Symbols

ITGB3; BDPLT2; CD61; GP3A; GPIIIa; GT

External IDs

OMIM: 173470 MGI: 96612 HomoloGene: 55444 ChEMBL: 207 GeneCards: ITGB3 Gene

Gene Ontology
Molecular function	• protein disulfide isomerase activity • receptor activity • platelet-derived growth factor receptor binding • protein binding • identical protein binding • vascular endothelial growth factor receptor 2 binding • cell adhesion molecule binding
Cellular component	• nucleus • plasma membrane • integral to plasma membrane • integrin complex • platelet alpha granule membrane • melanosome • alphav-beta3 integrin-vitronectin complex
Biological process	• positive regulation of protein phosphorylation • positive regulation of endothelial cell proliferation • platelet degranulation • protein folding • cell-substrate junction assembly • cell adhesion • cell-matrix adhesion • integrin-mediated signaling pathway • axon guidance • blood coagulation • positive regulation of endothelial cell migration • negative regulation of macrophage derived foam cell differentiation • negative regulation of lipid storage • smooth muscle cell migration • virus-host interaction • platelet activation • extracellular matrix organization • positive regulation of vascular endothelial growth factor receptor signaling pathway • activation of protein kinase activity • negative regulation of lipid transport • tube development • wound healing • regulation of bone resorption • negative regulation of low-density lipoprotein particle receptor biosynthetic process • positive regulation of peptidyl-tyrosine phosphorylation • negative regulation of lipoprotein metabolic process • leukocyte migration • angiogenesis involved in wound healing • platelet aggregation
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 17:
45.33 – 45.42 Mb

Chr 11:
104.61 – 104.67 Mb

PubMed search

Integrin beta-3 (β3) or CD61 is a protein that in humans is encoded by the ITGB3 gene.^[1] CD61 is a cluster of differentiation found on thrombocytes.

Structure and function

The ITGB3 protein product is the integrin beta chain beta 3. Integrins are integral cell-surface proteins composed of an alpha chain and a beta chain. A given chain may combine with multiple partners resulting in different integrins. Integrin beta 3 is found along with the alpha IIb chain in platelets. Integrins are known to participate in cell adhesion as well as cell-surface-mediated signaling.^[2]

Role in endometriosis

Defectively expressed β3 integrin subunit has been correlated with presence of endometriosis, and has been suggested as a putative marker of this condition.^[3]

Interactions

CD61 has been shown to interact with PTK2,^[4]^[5] ITGB3BP,^[6]^[7] TLN1^[8]^[9] and CIB1.^[10]

References

↑ Sosnoski DM, Emanuel BS, Hawkins AL, van Tuinen P, Ledbetter DH, Nussbaum RL, Kaos FT, Schwartz E, Phillips D, Bennett JS, et al. (August 1988). "Chromosomal localization of the genes for the vitronectin and fibronectin receptors alpha subunits and for platelet glycoproteins IIb and IIIa". J Clin Invest 81 (6): 1993–8. doi:10.1172/JCI113548. PMC 442653. PMID 2454952.
↑ "Entrez Gene: ITGB3 integrin, beta 3 (platelet glycoprotein IIIa, antigen CD61)".
↑ May, K. E.; Villar, J.; Kirtley, S.; Kennedy, S. H.; Becker, C. M. (2011). "Endometrial alterations in endometriosis: A systematic review of putative biomarkers". Human Reproduction Update 17 (5): 637–653. doi:10.1093/humupd/dmr013. PMID 21672902.
↑ Eliceiri, Brian P; Puente Xose S, Hood John D, Stupack Dwayne G, Schlaepfer David D, Huang Xiaozhu Z, Sheppard Dean, Cheresh David A (April 2002). "Src-mediated coupling of focal adhesion kinase to integrin alpha(v)beta5 in vascular endothelial growth factor signaling". J. Cell Biol. (United States) 157 (1): 149–60. doi:10.1083/jcb.200109079. ISSN 0021-9525. PMC 2173263. PMID 11927607. Cite uses deprecated parameters (help)
↑ Chung, J; Gao A G, Frazier W A (June 1997). "Thrombspondin acts via integrin-associated protein to activate the platelet integrin alphaIIbbeta3". J. Biol. Chem. (UNITED STATES) 272 (23): 14740–6. doi:10.1074/jbc.272.23.14740. ISSN 0021-9258. PMID 9169439. Cite uses deprecated parameters (help)
↑ Fujimoto, Tetsuro-Takahiro; Katsutani Shinya, Shimomura Takeshi, Fujimura Kingo (January 2002). "Novel alternatively spliced form of beta(3)-endonexin". Thromb. Res. (United States) 105 (1): 63–70. doi:10.1016/S0049-3848(01)00405-4. ISSN 0049-3848. PMID 11864709. Cite uses deprecated parameters (help)
↑ Shattil, S J; O'Toole T, Eigenthaler M, Thon V, Williams M, Babior B M, Ginsberg M H (November 1995). "Beta 3-endonexin, a novel polypeptide that interacts specifically with the cytoplasmic tail of the integrin beta 3 subunit". J. Cell Biol. (UNITED STATES) 131 (3): 807–16. doi:10.1083/jcb.131.3.807. ISSN 0021-9525. PMC 2120613. PMID 7593198. Cite uses deprecated parameters (help)
↑ Patil, S; Jedsadayanmata A, Wencel-Drake J D, Wang W, Knezevic I, Lam S C (October 1999). "Identification of a talin-binding site in the integrin beta(3) subunit distinct from the NPLY regulatory motif of post-ligand binding functions. The talin n-terminal head domain interacts with the membrane-proximal region of the beta(3) cytoplasmic tail". J. Biol. Chem. (UNITED STATES) 274 (40): 28575–83. doi:10.1074/jbc.274.40.28575. ISSN 0021-9258. PMID 10497223. Cite uses deprecated parameters (help)
↑ Calderwood, David A; Yan Boxu, de Pereda Jose M, Alvarez Begoña García, Fujioka Yosuke, Liddington Robert C, Ginsberg Mark H (June 2002). "The phosphotyrosine binding-like domain of talin activates integrins". J. Biol. Chem. (United States) 277 (24): 21749–58. doi:10.1074/jbc.M111996200. ISSN 0021-9258. PMID 11932255. Cite uses deprecated parameters (help)
↑ Naik, U P; Patel P M, Parise L V (February 1997). "Identification of a novel calcium-binding protein that interacts with the integrin alphaIIb cytoplasmic domain". J. Biol. Chem. (UNITED STATES) 272 (8): 4651–4. doi:10.1074/jbc.272.8.4651. ISSN 0021-9258. PMID 9030514. Cite uses deprecated parameters (help)

External links

CD61 Antigens at the US National Library of Medicine Medical Subject Headings (MeSH)
ITGB3 Info with links in the Cell Migration Gateway

PDB gallery

1jv2: CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN ALPHAVBETA3

1l5g: CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN AVB3 IN COMPLEX WITH AN ARG-GLY-ASP LIGAND

1m1x: CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN ALPHA VBETA3 BOUND TO MN2+

1m8o: Platelet integrin alfaIIb-beta3 cytoplasmic domain

1txv:

1ty3:

1ty5:

1ty6:

1ty7:

1tye: Structural basis for allostery in integrins and binding of ligand-mimetic therapeutics to the platelet receptor for fibrinogen

1u8c: A novel adaptation of the integrin PSI domain revealed from its crystal structure

v t e Proteins: clusters of differentiation (see also list of human clusters of differentiation)

1-50	CD1 a-c 1A 1D 1E CD2 CD3 γ δ ε CD4 CD5 CD6 CD7 CD8 a CD9 CD10 CD11 a b c d CD13 CD14 CD15 CD16 A B CD18 CD19 CD20 CD21 CD22 CD23 CD24 CD25 CD26 CD27 CD28 CD29 CD30 CD31 CD32 A B CD33 CD34 CD35 CD36 CD37 CD38 CD39 CD40 CD41 CD42 a b c d CD43 CD44 CD45 CD46 CD47 CD48 CD49 a b c d e f CD50

51-100	CD51 CD52 CD53 CD54 CD55 CD56 CD57 CD58 CD59 CD61 CD62 E L P CD63 CD64 A B C CD66 a b c d e f CD68 CD69 CD70 CD71 CD72 CD73 CD74 CD78 CD79 a b CD80 CD81 CD82 CD83 CD84 CD85 a d e h j k CD86 CD87 CD88 CD89 CD90 CD91 - CD92 CD93 CD94 CD95 CD96 CD97 CD98 CD99 CD100

101-150	CD101 CD102 CD103 CD104 CD105 CD106 CD107 a b CD108 CD109 CD110 CD111 CD112 CD113 CD114 CD115 CD116 CD117 CD118 CD119 CD120 a b CD121 a b CD122 CD123 CD124 CD125 CD126 CD127 CD129 CD130 CD131 CD132 CD133 CD134 CD135 CD136 CD137 CD138 CD140b CD141 CD142 CD143 CD144 CD146 CD147 CD148 CD150

151-200	CD151 CD152 CD153 CD154 CD155 CD156 a b c CD157 CD158 (a d e i k) CD159 a c CD160 CD161 CD162 CD163 CD164 CD166 CD167 a b CD168 CD169 CD170 CD171 CD172 a b g CD174 CD177 CD178 CD179 a b CD180 CD181 CD182 CD183 CD184 CD185 CD186 CD191 CD192 CD193 CD194 CD195 CD196 CD197 CDw198 CDw199 CD200

201-250	CD201 CD202b CD204 CD205 CD206 CD207 CD208 CD209 CDw210 a b CD212 CD213a 1 2 CD217 CD218 (a b) CD220 CD221 CD222 CD223 CD224 CD225 CD226 CD227 CD228 CD229 CD230 CD233 CD234 CD235 a b CD236 CD238 CD239 CD240CE CD240D CD241 CD243 CD244 CD246 CD247 - CD248 CD249

251-300	CD252 CD253 CD254 CD256 CD257 CD258 CD261 CD262 CD264 CD265 CD266 CD267 CD268 CD269 CD271 CD272 CD273 CD274 CD275 CD276 CD278 CD279 CD280 CD281 CD282 CD283 CD284 CD286 CD288 CD289 CD290 CD292 CDw293 CD294 CD295 CD297 CD298 CD299

301-350	CD300A CD301 CD302 CD303 CD304 CD305 CD306 CD307 CD309 CD312 CD314 CD315 CD316 CD317 CD318 CD320 CD321 CD322 CD324 CD325 CD326 CD328 CD329 CD331 CD332 CD333 CD334 CD335 CD336 CD337 CD338 CD339 CD340 CD344 CD349 CD350

Proteins: coagulation

Coagulation factors

Primary hemostasis	vWF platelet membrane glycoproteins: Ib (A B IX) IIb/IIIa (IIb IIIa) VI

Intrinsic pathway	HMWK/Bradykinin Prekallikrein/Kallikrein XII "Hageman" XI IX VIII

Extrinsic pathway	III "Tissue factor" VII

Common pathway	X V II "(Pro)thrombin" I "Fibrin" Fibrinogen (FGA, FGG) XIII

Coagulation inhibitors

Thrombolysis/fibrinolysis

M: MYL

cell/phys (coag, heme, immu, gran), csfs

rbmg/mogr/tumr/hist, sysi/epon, btst

drug (B1/2/3+5+6), btst, trns

Integrins

Alpha

Beta

Dimers

Cytoadhesin receptor:	Integrin alpha6beta4 Glycoprotein IIb/IIIa ITGA2B+ITGB3

Fibrinogen receptor:	Macrophage-1 antigen CD11b+CD18

Fibronectin receptor:	Integrin alpha2beta1 Integrin alpha4beta1 Integrin alpha5beta1

Leukocyte-adhesion receptor:	LFA-1 CD11a+CD18 Macrophage-1 antigen CD11b+CD18 Integrin alphaXbeta2 CD11c+CD18

Very late antigen receptor:	Integrin alpha1beta1 Integrin alpha2beta1 Integrin alpha3beta1 VLA-4 CD49d+CD29 Alpha-5 beta-1 Integrin alpha6beta1

Vitronectin receptor:	Alpha-v beta-3 Alpha-v beta-5

see also cell surface receptor deficiencies
B trdu: iter (nrpl/grfl/cytl/horl), csrc (lgic, enzr, gprc, igsr, intg, nrpr/grfr/cytr), itra (adap, gbpr, mapk), calc, lipd; path (hedp, wntp, tgfp+mapp, notp, jakp, fsap, hipp, tlrp)

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